DevT (Alr4674), resembling a Ser/Thr protein phosphatase, is essential for heterocyst function in the cyanobacterium Anabaena sp. PCC 7120

Por favor, use este identificador para citar o enlazar este ítem: http://hdl.handle.net/10045/15134
Información del item - Informació de l'item - Item information
Título: DevT (Alr4674), resembling a Ser/Thr protein phosphatase, is essential for heterocyst function in the cyanobacterium Anabaena sp. PCC 7120
Autor/es: Espinosa, Javier | Brunner, Thomas | Fiedler, Nicole | Forchhammer, Karl | Muro-Pastor, Alicia M. | Maldener, Iris
Grupo/s de investigación o GITE: Transducción de Señales en Bacterias
Centro, Departamento o Servicio: Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología | University of Tübingen. Interfaculty Institute for Microbiology and Infection Medicine, Organismic Interactions | University of Regensburg. Lehrstuhl fur Zellbiologie und Pflanzenphysiologie | Instituto de Bioquímica Vegetal y Fotosíntesis (CSIC-Universidad de Sevilla)
Palabras clave: Cyanobacteria | Anabaena
Área/s de conocimiento: Genética
Fecha de creación: 2010
Fecha de publicación: 2010
Editor: Society for General Microbiology
Cita bibliográfica: ESPINOSA MANZANO, Javier, et al. “DevT (Alr4674), resembling a Ser/Thr protein phosphatase, is essential for heterocyst function in the cyanobacterium Anabaena sp. PCC 7120”. Microbiology. 156 (2010). ISSN 1350-0872 (Paper in press)
Resumen: Heterocyst-forming cyanobacteria are able to perform oxygenic photosynthesis and nitrogen fixation simultaneously in the same filament, by restricting the highly O2 sensitive nitrogenase to specialized cells, the heterocysts. A remarkable change in morphology and metabolism accompanies the differentiation of heterocysts, which only occurs when no source of combined nitrogen is available. In the present study, we characterized DevT (Alr4674), a putative protein phosphatase from Anabaena PCC 7120. Mutants defective in devT are able to form morphologically mature heterocysts, which however cannot fix N2 and the mutant cannot survive without a source of combined nitrogen. DevT shows homology to phosphatases of the PPP family and displays a Mn2+-dependent phosphatase activity that can be inhibited by phosphatase inhibitors and oxidizing conditions. DevT is constitutively expressed both in vegetative cells and heterocysts, and is not regulated by NtcA. Heterocyst regulator HetR may exert a certain inhibition on expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. Therefore DevT plays a still unknown role in a late essential step of heterocyst differentiation.
Patrocinador/es: This work was supported by a grant from the Deutsche Forschungsgemeinschaft, DFG (MA1359/2-3). J. E. received a grant from the Ministerio de Ciencia e Innovación, Spain.
URI: http://hdl.handle.net/10045/15134
ISSN: 1350-0872 (Print) | 1465-2080 (Online)
DOI: 10.1099/mic.0.043398-0
Idioma: eng
Tipo: info:eu-repo/semantics/article
Derechos: This is an author manuscript that has been accepted for publication in Microbiology, copyright Society for General Microbiology, but has not been copy-edited, formatted or proofed. Cite this article as appearing in Microbiology. This version of the manuscript may not be duplicated or reproduced, other than for personal use or within the rule of 'Fair Use of Copyrighted Materials' (section 17, Title 17, US Code), without permission from the copyright owner, Society for General Microbiology. The Society for General Microbiology disclaims any responsibility or liability for errors or omissions in this version of the manuscript or in any version derived from it by any other parties. The final copy-edited, published article, which is the version of record, can be found at http://mic.sgmjournals.org, and is freely available without a subscription.
Revisión científica: si
Versión del editor: http://dx.doi.org/10.1099/mic.0.043398-0
Aparece en las colecciones:INV - TSB - Artículos de Revistas

Archivos en este ítem:
Archivos en este ítem:
Archivo Descripción TamañoFormato 
Thumbnailmic043398.pdf1,4 MBAdobe PDFAbrir Vista previa


Todos los documentos en RUA están protegidos por derechos de autor. Algunos derechos reservados.